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Science 12 February 1993:
Vol. 259. no. 5097, pp. 977 - 980
DOI: 10.1126/science.8438158
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Articles

Science, Vol 259, Issue 5097, 977-980
Copyright © 1993 by American Association for the Advancement of Science

articles

Carboxyl methylation of Ras-related proteins during signal transduction in neutrophils

MR Philips, MH Pillinger, R Staud, C Volker, MG Rosenfeld, G Weissmann, and JB Stock

Department of Medicine, New York University Medical Center, NY 10016.

In human neutrophils, as in other cell types, Ras-related guanosine triphosphate-binding proteins are directed toward their regulatory targets in membranes by a series of posttranslational modifications that include methyl esterification of a carboxyl-terminal prenylcysteine residue. In intact cells and in a reconstituted in vitro system, the amount of carboxyl methylation of Ras-related proteins increased in response to the chemoattractant N-formyl-methionyl-leucyl-phenylalanine (FMLP). Activation of Ras-related proteins by guanosine-5'-O-(3-thiotriphosphate) had a similar effect and induced translocation of p22rac2 from cytosol to plasma membrane. Inhibitors of prenylcysteine carboxyl methylation effectively blocked neutrophil responses to FMLP. These findings suggest a direct link between receptor-mediated signal transduction and the carboxyl methylation of Ras-related proteins.


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